DataSheet1_Quantitative proteomic analysis reveals the effects of mu opioid agonists on HT22 cells.ZIP

Introduction: At present, the mu opioid receptor is the most important neuroaesthetics receptor in anesthesiology research, and the damage that it does to the nervous system is unknown.Methods: We investigated the effects of loperamide, an agonist of the mu opioid receptor, on protein expression in HT22 cells using stable isotope labeling of amino acids in cell culture (SILAC), immobilized metal affinity chromatography (IMAC) enrichment, and high-resolution liquid chromatography-tandem mass spectrometry (LC-MS/MS). A total of 7,823 proteins were identified.Results and Discussion: Bioinformatic analysis revealed that mu opioid receptor agonism can induce distinct changes in the proteome of HT22 cells. These findings improve our understanding of narcotic drugs.</p

Additional file 1 of Assessment of the efficiency of synergistic photocatalysis on penicillin G biodegradation by whole cell Paracoccus sp

Additional file 1: Table S1. Degradation capability of Penicillin G by different strain species as reported from previous literatures and this study. Fig. S1a-c: Structure of the identified metabolites of peak Nos. 2 (a), 3 (a), 4 (b), and 5 (c) by LC–MS analysis. Peak Nos. 2 and 3 in HPLC: Potassium 2-(carboxy(2-phenylacetamido)methyl)-5,5-dimethylthiazolidine-4-carboxylate and potassium 2-(4-carboxy-5,5-dimethylthiazolidin-2-yl)-2-(2-phenylacetamido) acetate. Peak No. 4 in HPLC: Phenylacetic acid. Peak No. 5 in HPLC: Mixture of two isomers, 2-(amino(carboxyl)methyl)-5,5-dimethylthiazolidine-4-carboxylic acid. Fig. S2a-b: 1H NMR (a) and 13C NMR (b) spectra of potassium 2-(carboxy(2-phenylacetamido)methyl)-5,5-dimethylthiazolidine-4-carboxylate and potassium 2-(4-carboxy-5,5-dimethylthiazolidin-2-yl)-2-(2-phenylacetamido) acetate. 1H NMR (500 MHz, D2O) δ:7.34–7.45 (m, 10H); 5.07–5.06 (d, J = 3 Hz, 1H); 5.05–5.06 (d, J = 6 Hz, 1H); 4.79–4.78 (d, J = 3 Hz, 2H), 4.25–4.24 (d, J = 6 Hz, 1H); 3.81–3.80 (d, J = 4.0 Hz, 2H); 3.72–3.70 (d, J = 12 Hz, 1H); 3.43–3.42 (d, J = 3.5 Hz, 2H); 1.57 (s, 3H); 1.51 (s, 3H); 1.23 (s,3H); 1.05 (s, 3H).13C NMR (125 MHz, D2O) δ:176.17, 175.58, 175.24, 174.93, 174.86, 174.30, 135.01, 134.50, 129.65(2C), 129.49(2C), 129.27(2C), 129.04(2C), 127.61, 127.42, 75.84, 75.28, 67.00, 66.02, 60.01, 58.61, 58.45, 55.24, 42.51, 42.46, 27.98, 27.75, 26.75, 26.33. LC–MS (m/z): 391.3[M + 1]+ (cald. For C16H19KN2O5S, 390.1), 353.2[M` + 1]+ (cald for C16H20N2O5S, 352.1). Fig. S3a-b: 1H NMR (a) and 13C NMR (b) spectra of phenylacetic acid. 1H NMR (500 MHz, D2O) δppm: 7.42–7.32 (m, 5H); 3.73 (s, 2H).13CNMR (125 MHz, D2O) δppm: 177.01, 134.17, 129.38(2C), 128.79(2C), 127.27, 40.54. LC–MS (m/z): 137.3[M + 1]+ (cald. For C8H8O2, 136.05). Fig. S4a-b: 1H NMR (a) and 13C NMR (b) spectra of 5,5-dimethylthiazolidine. 1H NMR (500 MHz, D2O) δ: 5.06–5.05 (d, J = 4.5 Hz, 1H); 4.85–4.83 (d, J = 10.0 Hz, 1H); 3.97–3.96 (d, J = 4.0 Hz, 1H); 3.64–3.62 (d, J = 10.0 Hz, 1H); 3.56 (s, 2H); 3.47 (s, 1H); 3.19 (s,1H); 1.45 (s, 3H); 1.44 (s, 3H); 1.19 (s, 3H); 1.13(s, 3H). 13C NMR (125 MHz, D2O) δ: 176.34, 174.38, 171.85, 171.20, 74.47, 74.00, 63.59, 63.29, 59.31, 58.68, 56.80, 56.39, 29.29, 26.06, 26.02, 25.94. LC–MS (m/z): 235.1 [M + 1]+ (cald for C8H14N2O4S, 234.07)

Supplementary Information for Chemodrug-gated mesoporous nanoplatform for NIR light controlled drug release and synergistic chemophotothermal therapy of tumors

Figure S1. Nitrogen absorption isotherms of GNR@mSiO2. Fig S2 (a) UV-Vis curves of DOX at different concentrations. (b) Calibration curve used for estimation of DOX. Figure S3. FTIR spectra of GNR@mSiO2 and GNR@mSiO2-DOX/PFP@PDA. Figure S4. Microscopic images of microbubbles at different concentrations. Figure S5. Release profiles from GNR@mSiO2-DOX/PFP at different pH values with or without NIR. Figure S6. Cell cytotoxicity of normal cells (BALB/3T3) without NIR or with NIR (power density of 2 W/cm2) for 5 min. Figure S7. (a) H&E staining images of tumor sections after different treatments. (b) H&E-stained major organ tissue slices after different treatments. (Scale bar = 150 μm

Table1_Quantitative proteomic analysis reveals the effects of mu opioid agonists on HT22 cells.XLSX

Introduction: At present, the mu opioid receptor is the most important neuroaesthetics receptor in anesthesiology research, and the damage that it does to the nervous system is unknown.Methods: We investigated the effects of loperamide, an agonist of the mu opioid receptor, on protein expression in HT22 cells using stable isotope labeling of amino acids in cell culture (SILAC), immobilized metal affinity chromatography (IMAC) enrichment, and high-resolution liquid chromatography-tandem mass spectrometry (LC-MS/MS). A total of 7,823 proteins were identified.Results and Discussion: Bioinformatic analysis revealed that mu opioid receptor agonism can induce distinct changes in the proteome of HT22 cells. These findings improve our understanding of narcotic drugs.</p

Network pharmacology and experimental validation to explore the molecular mechanisms of Bushen Huoxue for the treatment of premature ovarian insufficiency

Bushen Huoxue (BSHX) has been applied in clinical traditional Chinese medicine treatment, and has definitive clinical efficacy in the treatment of Premature Ovarian Insufficiency (POI) in China. However, little is known of the underlying mechanism of BSHX. The purpose of this paper is to study the pharmacological mechanisms of BSHX acting on POI based on a pharmacology and experimental validation. The pharmacological database of chinese medicine system and analysis platform (TCMSP) were used to search the effective active ingredients and potential action targets of BSHX. Drugbank, Online Mendelian Inheritance in Man (OMIM), Genecards, and Disgenet databases were used to obtain relevant targets of POI. Gene Ontology (GO) enrichment, Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway enrichment, and the visual network of protein-protein interaction network were constructed by FunRich3.1. Pymol software, and Auto Dock tools 1.5.6 were used for molecular docking. Murine model of POI was used to further investigate the mechanism of BSHX against on POI. Finally, 127 active compounds were collected from TCMSP database, and 215 active targets were identified. There were 1366 targets related to POI and 99 targets of BSHX for the treatment of POI. Quercetin, kaempferol, and stigmasterol were recognized as the most effective compounds corresponding to targets. The top three genes according to degree value are TP53, Akt1, and VEGFA. Further, the results of GO and KEGG enrichment analysis revealed that those core targets were mainly enriched on TRAIL and TGF-β receptor signaling. The results of molecular docking showed that stigmasterol had good binding ability to Akt1. Moreover, experimental validation suggests that BSHX significantly Increased the expression of TGF-β1 and Smad2/3, regulating the release of serum sex hormones, which include Follicular stimulating hormone (FSH), Estradiol (E2), and Antimullerin hormone (AMH). BSHX treats POI by regulating TGF-β1 and Smad2/3 signaling pathways; Quercetin, kaempferol, and stigmasterol were the most effective compounds in BSHX.</p

Simultaneous production of propionic acid and vitamin B12 from corn stalk hydrolysates by <i>Propionibacterium freudenreichii</i> in an expanded bed adsorption bioreactor

Vitamin B12 and propionic acid that were simultaneous produced by Propionibacterium freudenreichii are both favorable chemicals widely used in food preservatives, medicine, and nutrition. While the carbon source and propionic acid accumulation reflected fermentation efficiency. In this study, using corn stalk as a carbon source and fed-batch fermentation process in an expanded bed adsorption bioreactor was studied for efficient and economic biosynthesis of acid vitamin B12 and propionic. With liquid hot water pretreated corn stalk hydrolysates as carbon source, 28.65 mg L−1 of vitamin B12 and 17.05 g L−1 of propionic acid were attained at 168 h in batch fermentation. In order to optimize the fermentation outcomes, fed-batch fermentation was performed with hydrolyzed corn stalk in expanded bed adsorption bioreactor (EBAB), giving 47.6 mg L−1 vitamin B12 and 91.4 g L−1 of propionic acid at 258 h, which correspond to product yields of 0.37 mg g−1 and 0.75 g g−1, respectively. The present study provided a promising strategy for economically sustainable production of vitamin B12 and propionic acid by P. freudenreichii fermentation using biomass cornstalk as carbon source and expanded bed adsorption bioreactor.</p

Novel One‑, Two‑, and Three-Dimensional Selenidostannates Templated by Iron(II) Complex Cation

The novel iron selenidostannates [Fe­(bipy)₃]­Sn₄Se₉·2H₂O (<b>1</b>) and [Fe­(bipy)₃]₂[Sn₃Se₇]₂·bipy·2H₂O (<b>2</b>) (bipy = bipyridine) were prepared by the reactions of Sn, Se, FeCl₂·4H₂O, bipy, and dien with/without KSCN under hydrothermal conditions (dien = diethylenetriamine). In <b>1</b>, four SnSe₅ units condense via edge sharing to form the novel 3-D framework selenidostannate _∞³[Sn₄Se₉^2–] containing an interpenetrating channel system. The [Fe­(bipy)₃]²⁺ cations are accommodated in the different channels according to the conformation of the [Fe­(bipy)₃]²⁺ cation. In <b>2</b>, three SnSe₅ units share edges to form a 2-D _∞²[Sn₃Se₇^2–] layered anion, while two SnSe₅ units and one SnSe₄ unit are connected via edge sharing, forming a 1-D _∞¹[Sn₃Se₇^2–] chainlike anion. The _∞¹[Sn₃Se₇^2–], [Fe­(bipy)₃]²⁺, bipy, and H₂O species are embedded between the _∞²[Sn₃Se₇^2–] layers. <b>2</b> is the first example of a selenidostannate constructed by both _∞²[Sn₃Se₇^2–]­and _∞¹[Sn₃Se₇^2–] anions. The coexistence of 1-D _∞¹[Sn₃Se₇^2–] and 2-D _∞²[Sn₃Se₇^2–] anions in <b>2</b> might support the possible reaction mechanism that the _∞²[Sn₃Se₇^2–] anions are formed by condensation of the _∞¹[Sn₃Se₇^2–] chains. <b>1</b> and <b>2</b> exhibit band gaps at 1.43 and 2.01 eV, respectively

Solvothermal syntheses and characterizations of polysulfido-thioantimonate and thioantimonate templated by Co-phen complex cation

<div><p>Polysulfido-thioantimonate [Co(phen)₃][Sb₄S₅(S₄)₂] (<b>1</b>), thioantimonates [Co(phen)₃]₂Sb₁₈S₂₉ (<b>2</b>), and [H₃O][Co(phen)₃]SbS₄·9H₂O (<b>3</b>) (phen = 1,10-phenanthroline) were prepared using [Co(phen)₃]²⁺ formed <i>in situ</i> as a structure directing agent in 80 and 50% CH₃OH aqueous solution or water solution, respectively. In <b>1</b>, eight Sb³⁺ ions are connected by ten μ-S²⁻ and four μ- bridging ligands to form a circular polysulfide thioantimonate anion [Sb₈S₁₀(S₄)₄]⁴⁻ which contains a sixteen-membered Sb₈S₈ heteroring. The Sb³⁺ ions are in trigonal pyramidal SbS₃ or trigonal bipyramidal <i>ψ</i>-SbS₄ geometries. In <b>2</b>, sixteen SbS₃ and two <i>ψ</i>-SbS₄ units are interconnected by sharing S atoms to form a 3-D [Sb₁₈S₂₉⁴⁻]_∞ framework containing an interpenetrating channel system, in which the [Co(phen)₃]²⁺ complexes are enclosed. In <b>3</b>, by O–H⋯O and O–H⋯S H-bonding, [SbS₄]³⁻,·H₂O and H₃O⁺ are interconnected into a anionic layer, which contains a (H₂O)₆ water cluster. The [Co(phen)₃]²⁺ complexes are located between the layers. The syntheses of <b>1</b>–<b>3</b> show the influences of different solvents on the Co/Sb/S/phen system. The optical band gaps of <b>1</b>–<b>3</b> are 2.02, 2.11, and 2.27 eV, respectively.</p></div

Curcumin analogues exert potent inhibition on human and rat gonadal 3β-hydroxysteroid dehydrogenases as potential therapeutic agents: structure-activity relationship and in silico docking

Curcuminoids are functional food additives, and the effect on gonadal hormone biosynthesis remains unclear. Gonads contain 3β-hydroxysteroid dehydrogenase isoforms, h3β-HSD2 (humans) and r3β-HSD1 (rats), which catalyse pregnenolone into progesterone. The potency and mechanisms of curcuminoids to inhibit 3β-HSD activity were explored. The inhibitory potency was bisdemethoxycurcumin (IC50, 1.68 µM) >demethoxycurcumin (3.27 µM) > curcumin (13.87 µM) > tetrahydrocurcumin (109.0 µM) > dihydrocurcumin and octahydrocurcumin on KGN cell h3β-HSD2, while that was bisdemethoxycurcumin (1.22 µM) >demethoxycurcumin (2.18 µM) > curcumin (4.12 µM) > tetrahydrocurcumin (102.61 µM) > dihydrocurcumin and octahydrocurcumin on testicular r3β-HSD1. All curcuminoids inhibited progesterone secretion by KGN cells under basal and forskolin-stimulated conditions at >10 µM. Docking analysis showed that curcuminoids bind steroid-active site with mixed or competitive mode. In conclusion, curcuminoids inhibit gonadal 3β-HSD activity and de-methoxylation of curcumin increases inhibitory potency and metabolism of curcumin by saturation of carbon chain losses inhibitory potency.</p